Membrane structure and dynamics as viewed by solid-state NMR spectroscopy.
The purpose of the present study is the investigation of the structure and dynamics of biological membranes using solid-state nuclear magnetic resonance (NMR) spectroscopy. Two approaches are used in our laboratory. The first involves the measurement of high-resolution 13C and 1H spectra obtained by the magic angle spinning (MAS) technique while the second approach involves the measurement of 31P and 2H powder spectra in static samples. This paper will present some recent results obtained by high-resolution solid-state 1H NMR on the conformation of gramicidin A incorporated in a phosphatidylcholine bilayers. More specifically, we were able to observe changes in the gramicidin spectra as a function of the cosolubilization solvent initially used to prepare the samples. The interaction between lipid bilayers and an anticancer drug derived from chloroethylurea was also investigated using proton NMR spectroscopy. Finally, we have studied the interaction between cardiotoxin, a toxic protein extracted from snake venom, and negatively charged lipid bilayers using 31P solid-state NMR spectroscopy.
Auger
M
M
Département de Chimie, CERSIM, Université Laval, Québec, Canada. Michele.auger@chm.ulaval.ca
D002462:Cell Membrane / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism; D004179:Cobra Cardiotoxin Proteins / Q000633:toxicity; D008051:Lipid Bilayers / Q000737:chemistry* / Q000378:metabolism; D008565:Membrane Proteins / Q000737:chemistry* / Q000187:drug effects; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010758:Phosphorus; D013816:Thermodynamics
D004179:Cobra Cardiotoxin Proteins; D008051:Lipid Bilayers; D008565:Membrane Proteins; D010758:Phosphorus